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2nul

From Proteopedia

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[[Image:2nul.jpg|left|200px]]
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{{STRUCTURE_2nul| PDB=2nul | SCENE= }}
{{STRUCTURE_2nul| PDB=2nul | SCENE= }}
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'''PEPTIDYLPROLYL ISOMERASE FROM E. COLI'''
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===PEPTIDYLPROLYL ISOMERASE FROM E. COLI===
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==Overview==
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The structure of the unliganded form of the Escherichia coli cytoplasmic peptidyl-prolyl isomerase (ppiB gene product) in a new crystal form was determined by the molecular replacement method and refined to an R-factor of 16.1% at 2.1 A resolution. The enzyme crystallized in the orthorhombic C2221 space group with unit cell dimensions of a=44.7 A, b=68.2 A and c=102.0 A. Comparison with the reported structure of the enzyme complexed with the tripeptide substrate succinyl-Ala-Pro-Ala-p-nitroanilide revealed subtle changes that occur upon complex formation. There is evidence to suggest that two surface loops have significantly reduced mobility in the complexed structure.
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{{ABSTRACT_PUBMED_9268657}}
==About this Structure==
==About this Structure==
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[[Category: Isomerase]]
[[Category: Isomerase]]
[[Category: Rotamase]]
[[Category: Rotamase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:55:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:25:53 2008''

Revision as of 10:25, 29 July 2008

Image:2nul.png

Template:STRUCTURE 2nul

PEPTIDYLPROLYL ISOMERASE FROM E. COLI

Template:ABSTRACT PUBMED 9268657

About this Structure

2NUL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: evidence for decreased mobility of loops upon complexation., Edwards KJ, Ollis DL, Dixon NE, J Mol Biol. 1997 Aug 15;271(2):258-65. PMID:9268657

Page seeded by OCA on Tue Jul 29 13:25:53 2008

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